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Water scaffolding in collagen: Implications on protein dynamics as revealed by solid-state NMR
Article first published online: 18 DEC 2013
Copyright © 2013 The Authors Biopolymers Published by Wiley Periodicals, Inc.
This is an open access article under the terms of the Creative Commons Attribution License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.
Volume 101, Issue 3, pages 246–256, March 2014
How to Cite
Aliev, A. E. and Courtier-Murias, D. (2014), Water scaffolding in collagen: Implications on protein dynamics as revealed by solid-state NMR. Biopolymers, 101: 246–256. doi: 10.1002/bip.22330
- Issue published online: 18 DEC 2013
- Article first published online: 18 DEC 2013
- Accepted manuscript online: 19 JUN 2013 10:49PM EST
- Manuscript Accepted: 12 JUN 2013
- Manuscript Revised: 5 JUN 2013
- Manuscript Received: 17 MAY 2013
- The UK 850 MHz solid-state NMR Facility—EPSRC and BBSRC
- University of Warwick funding through Birmingham Science City Advanced Materials Projects 1 and 2 supported by Advantage West Midlands (AWM)
- the European Regional Development Fund (ERDF)
- solid-state NMR
Solid-state NMR studies of collagen samples of various origins confirm that the amplitude of collagen backbone and sidechain motions increases significantly on increasing the water content. This conclusion is supported by the changes observed in three different NMR observables: (i) the linewidth dependence on the 1H decoupling frequency; (ii) 13C CSA changes for the peptide carbonyl groups, and (iii) dephasing rates of 1H-13C dipolar couplings. In particular, a nearly threefold increase in motional amplitudes of the backbone librations about C-Cα or N-Cα bonds was found on increasing the added water content up to 47 wt%D2O. On the basis of the frequencies of NMR observables involved, the timescale of the protein motions dependent on the added water content is estimated to be of the order of microseconds. This estimate agrees with that from wideline T2 1H NMR measurements. Also, our wideline 1H NMR measurements revealed that the timescale of the microsecond motions in proteins reduces significantly on increasing the added water content, i.e., an ∼15-fold increase in protein motional frequencies is observed on increasing the added water content to 45 wt% D2O. The observed changes in collagen dynamics is attributed to the increase in water translational diffusion on increasing the amount of added water, which leads to more frequent “bound water/free water” exchange on the protein surface, accompanied by the breakage and formation of new hydrogen bonds with polar functionalities of protein. © 2013 Wiley Periodicals, Inc. Biopolymers 101: 246–256, 2014.